Papain-catalyzed synthesis of phenylhydrazides of N-acylamino acids

1984 ◽  
Vol 49 (11) ◽  
pp. 2557-2561 ◽  
Author(s):  
Václav Čeřovský ◽  
Karel Jošt

Phenylhydrazides of Nα-acyl derivatives of all coded amino acids, except proline, were prepared by papain (E.C. 3.4.22.2)-catalyzed synthesis. Comparison of yields affords information about the suitability of the amino acid in position P1 in papain-catalyzed syntheses of peptides.

1987 ◽  
Vol 33 (7) ◽  
pp. 577-582 ◽  
Author(s):  
A. Paquet ◽  
K. Rayman

Several N-acyl derivatives of D-tryptophan, D-alanine, D-methionine, D-valine, and D-aspartic acid were synthesized in high yields using the succinimidyl ester method and examined for their antibotulinal properties. In conjunction with 60 ppm of sodium nitrite, sorbyl-D-tryptophan, sorbyl-D-alanine, myristoyl-D-aspartic acid, and glycyl-D-alanine were highly inhibitory. In the absence of sodium nitrite, the N-acyl derivatives of the D-amino acids were not inhibitory. On its own, 60 ppm of sodium nitrite was only slightly inhibitory. Sorbyl-L-tryptophan and sorbyl-L-alanine had no effect in the presence or absence of 60 ppm of sodium nitrite.


2003 ◽  
Vol 58 (5-6) ◽  
pp. 366-370 ◽  
Author(s):  
Nijole Dirvianskytė ◽  
Juozapas Straukas ◽  
Valdemaras Razumas ◽  
Eugenius Butkus

Abstract Synthesis of N- and O-acyl derivatives of ᴅʟ-serine and threo-ᴅʟ-phenylserine was accomplished by a regioselective acylation of the corresponding amino acid. The residues introduced into amino acid structure contain hydrophobic long chain or aromatic, namely lauroyl, myristoyl and phenylacetyl moieties. The fungicidal activity against six strains of fungi was studied. Several compounds were found to be effective against growth of fungi, and Omyristoyl- ᴅʟ-serine 2 and N-phenylacetyl-threo-ᴅʟ-phenylserine 8 completely inhibited the growth of the mycelium of the fungus Verticillium dahliae.


1980 ◽  
Vol 11 (15) ◽  
Author(s):  
N. B. TARUSOVA ◽  
I. A. GANDURINA ◽  
YU. N. ZHUKOV ◽  
G. M. YAKOVLEVA ◽  
R. M. KHOMUTOV

1960 ◽  
Vol 38 (7) ◽  
pp. 1135-1140 ◽  
Author(s):  
I. Levi ◽  
A. E. Koller ◽  
G. Laflamme ◽  
J. W. R. Weed

The N-dichloroacetyl derivatives of DL-serine and DL-threonine were prepared by the Schotten–Baumann reaction from the amino acids and dichloroacetyl chloride. Negative ninhydrin tests coupled with elementary analyses indicated that only the amino group was acylated. The ester derivatives of these compounds were prepared either by esterification of the N-dichloroacetyl-DL-amino acid with diazomethane or by the reaction of the amino acid ester with dichloroacetyl chloride in the presence of triethylamine. The sodium salts and the esters were tested for antitumor activity against sarcoma 37 in mice and Walker carcinoma 256 in rats. In both cases regression of the tumors was obtained.


1968 ◽  
Vol 110 (2) ◽  
pp. 289-296 ◽  
Author(s):  
K. B. M. Reid ◽  
P T Grant ◽  
A. Youngson

1. S-Aminoethylcysteinyl derivatives of the A and B chains of cod insulin were prepared from the individual S-sulpho chains. 2. Studies on small peptides derived from the S-aminoethylated peptide chains by treatment with trypsin allowed the amino acid sequences in the region of the cysteinyl residues of the A and B peptide chains to be defined. 3. The six amide groups in cod insulin were located by complete digestion of small peptides from the A and B chains with aminopeptidase followed by amino acid analyses. 4. The results, together with previous studies on the oxidized A and B chains, define the sequences of the 51 amino acids that constitute cod insulin.


Author(s):  
N. B. Tarusova ◽  
I. A. Gandurina ◽  
Yu. N. Zhukov ◽  
G. M. Yakovleva ◽  
R. M. Khomutov

1975 ◽  
Vol 53 (9) ◽  
pp. 1005-1009 ◽  
Author(s):  
C. S. Tsai ◽  
N. L. Fraser ◽  
H. Avdovich ◽  
J. P. Farant

Proton magnetic spectra of 3-phenyl-2-thiohydantoin derivatives of common amino acids in deuterated dimethyl sulfoxide were recorded. Spectral data pertaining to characteristic protons for diagnostic purpose were compiled. Their application to the N-terminal amino acid analysis of peptide by Edman degradation was examined.


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